1gpj
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Processes vital to life such as respiration and photosynthesis critically | + | Processes vital to life such as respiration and photosynthesis critically depend on the availability of tetrapyrroles including hemes and chlorophylls. tRNA-dependent catalysis generally is associated with protein biosynthesis. An exception is the reduction of glutamyl-tRNA to glutamate-1-semialdehyde by the enzyme glutamyl-tRNA reductase. This reaction is the indispensable initiating step of tetrapyrrole biosynthesis in plants and most prokaryotes. The crystal structure of glutamyl-tRNA reductase from the archaeon Methanopyrus kandleri in complex with the substrate-like inhibitor glutamycin at 1.9 A resolution reveals an extended yet planar V-shaped dimer. The well defined interactions of the inhibitor with the active site support a thioester-mediated reduction process. Modeling the glutamyl-tRNA onto each monomer reveals an extensive protein-tRNA interface. We furthermore propose a model whereby the large void of glutamyl-tRNA reductase is occupied by glutamate-1-semialdehyde-1,2-mutase, the subsequent enzyme of this pathway, allowing for the efficient synthesis of 5-aminolevulinic acid, the common precursor of all tetrapyrroles. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Beier, V.]] | [[Category: Beier, V.]] | ||
[[Category: Bringemeier, I.]] | [[Category: Bringemeier, I.]] | ||
| - | [[Category: Heinz, D | + | [[Category: Heinz, D W.]] |
[[Category: Jahn, D.]] | [[Category: Jahn, D.]] | ||
[[Category: Moser, J.]] | [[Category: Moser, J.]] | ||
| - | [[Category: Schubert, W | + | [[Category: Schubert, W D.]] |
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: GMC]] | [[Category: GMC]] | ||
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[[Category: trna-dependent tetrapyrrole biosynthesis]] | [[Category: trna-dependent tetrapyrrole biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:36 2008'' |
Revision as of 10:52, 21 February 2008
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GLUTAMYL-TRNA REDUCTASE FROM METHANOPYRUS KANDLERI
Overview
Processes vital to life such as respiration and photosynthesis critically depend on the availability of tetrapyrroles including hemes and chlorophylls. tRNA-dependent catalysis generally is associated with protein biosynthesis. An exception is the reduction of glutamyl-tRNA to glutamate-1-semialdehyde by the enzyme glutamyl-tRNA reductase. This reaction is the indispensable initiating step of tetrapyrrole biosynthesis in plants and most prokaryotes. The crystal structure of glutamyl-tRNA reductase from the archaeon Methanopyrus kandleri in complex with the substrate-like inhibitor glutamycin at 1.9 A resolution reveals an extended yet planar V-shaped dimer. The well defined interactions of the inhibitor with the active site support a thioester-mediated reduction process. Modeling the glutamyl-tRNA onto each monomer reveals an extensive protein-tRNA interface. We furthermore propose a model whereby the large void of glutamyl-tRNA reductase is occupied by glutamate-1-semialdehyde-1,2-mutase, the subsequent enzyme of this pathway, allowing for the efficient synthesis of 5-aminolevulinic acid, the common precursor of all tetrapyrroles.
About this Structure
1GPJ is a Single protein structure of sequence from Methanopyrus kandleri with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis., Moser J, Schubert WD, Beier V, Bringemeier I, Jahn D, Heinz DW, EMBO J. 2001 Dec 3;20(23):6583-90. PMID:11726494
Page seeded by OCA on Thu Feb 21 12:52:36 2008
